ID   YTYK1_DICDI             Reviewed;         352 AA.
AC   Q54G28;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Probable tyrosine-protein kinase DDB_G0290471;
DE            EC=2.7.10.2;
GN   ORFNames=DDB_G0290471;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Tyr protein
CC       kinase family. {ECO:0000305}.
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DR   EMBL; AAFI02000163; EAL62251.1; -; Genomic_DNA.
DR   RefSeq; XP_635744.1; XM_630652.1.
DR   AlphaFoldDB; Q54G28; -.
DR   SMR; Q54G28; -.
DR   STRING; 44689.DDB0229850; -.
DR   PaxDb; Q54G28; -.
DR   PRIDE; Q54G28; -.
DR   EnsemblProtists; EAL62251; EAL62251; DDB_G0290471.
DR   GeneID; 8627663; -.
DR   KEGG; ddi:DDB_G0290471; -.
DR   dictyBase; DDB_G0290471; -.
DR   eggNOG; KOG0192; Eukaryota.
DR   HOGENOM; CLU_788522_0_0_1; -.
DR   InParanoid; Q54G28; -.
DR   OMA; WFELITH; -.
DR   PhylomeDB; Q54G28; -.
DR   PRO; PR:Q54G28; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN           1..352
FT                   /note="Probable tyrosine-protein kinase DDB_G0290471"
FT                   /id="PRO_0000355145"
FT   DOMAIN          51..333
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         57..65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   352 AA;  40829 MW;  49481817D4103A3D CRC64;
     MEIVINNISG LNNSFNNNNN SNNNDENEIN FNLIKESIVN FKLWDINNKQ IEYVCRLGSG
     SLCRVYKGRL NGKPVAIKVF SPIRFEEFKT EFLMMQSLRS SPFLISFYGV SIVEEPQKQC
     YCIITEFCSR DSLYHIMTDR LIEIGWNRFF QFSMQIILGL QSLHNRKPKP IVHRDVTSLN
     ILVNEDWECK ISNFSASRFN CLNTEYINSN NQNKSFAFCS PESSDFQDID DDYTSLSSSI
     TSKSDIYSFG IIMFELISRI INGEYSHPFS EFKDIKNDFQ LLLSSKNGLR PSLPNICPEP
     LEKLYKQCVD QSPLNRPSCE EVIISLNQIR SFYLLPQTKK SWDNLVLKNK CK